H2N2V1, Main, Exploration, bibRecord, 000D13

Structural basis of influenza virus neutralization

Identifieur interne : 000D13 ( Main/Exploration ); précédent : 000D12; suivant : 000D14

Structural basis of influenza virus neutralization

Auteurs : Thomas Han [États-Unis] ; Wayne A. Marasco [États-Unis]

Source :

Annals of the New York Academy of Sciences [ 0077-8923 ] ; 2011-01.

RBID : ISTEX:57880EBAE12FE3A2EF1600A8DECAF26E7CD8B046

English descriptors

Teeft :
- Acad, Acta virol, Amino, Amino acid changes, Amino acid variations, Amino acids, Antibody, Antibody neutralization, Antigenic, Antigenic drift, Antigenic shift, Antigenic sites, Antigenic structure, Antigenic variation, Antigenic variations, Avian, Avian viruses, Biol, Bnabs, Cancer immunology, Cancer institute, Carbonyl oxygen, Cell surface, Cleavage, Conformational changes, Crystal structures, Different subtypes, Endosomal membrane, Epitope, Fusion activity, Fusion peptide, Fusion peptide chain, Fusion process, Gene segments, Globular, Globular head, Globular head region, Haemagglutinin, Heavy chain, Helix, Hemagglutinin, Hemagglutinin figure, Hydrogen bond, Hydrophobic, Hydrophobic pocket, Immune, Immune responses, Immune system, Immunogen, Marasco, Marasco antibodies, Marasco figure, Membrane fusion, Monoclonal antibodies, Multiple subtypes, Mutant, Mutation, Nabs, Natural infection, Neutralization, Neutralization epitopes, Neutralizing, Neutralizing antibodies, Neutralizing antibody, Pandemic, Peptide, Plasma membrane, Population level, Proteolytic cleavage, Receptor, Receptor binding, Receptor binding region, Receptor binding site, Residue, Ribbon diagram, Same color, Seasonal vaccines, Side chain, Steric hindrance, Structural basis, Structural information, Subtypes, Subunit, Surface area, Universal vaccine, Vaccine, Vaccine immunogens, Vaccine strain selection, Vaccine strains, Vaccine strategies, Viral, Viral evolution, Virol, Virology, Virus, Virus entry, Virus evolution, Virus haemagglutinin, Virus hemagglutinin, Virus infectivity, Virus neutralization, Virus pathogenicity, Virus vaccine, York academy.

Abstract

Although seasonal influenza vaccines play a valuable role in reducing the spread of virus at the population level, ongoing viral evolution to evade immune responses remains problematic. No current vaccines elicit enduring protection in the face of emerging and re‐emerging influenza viruses that are rapidly undergoing antigenic drift. Eliciting broadly cross‐neutralizing antibody (nAb) responses against influenza virus is a crucial goal for seasonal and pandemic influenza vaccine preparation. Recent three‐dimensional structure information obtained from crystallization of influenza antigens in complex with nAbs has provided a framework for interpreting antibody‐based viral neutralization that should aid in the design of vaccine immunogens. Here, we will review current knowledge of the structure‐based mechanisms contributing to the neutralization and neutralization escape of influenza viruses. We will also explore the potential for this structure‐based approach to overcome the obstacles in developing the highly desired “universal” influenza vaccine.

Url:

DOI: 10.1111/j.1749-6632.2010.05829.x

Affiliations:

Le document en format XML

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<term>Amino acid variations</term>
<term>Amino acids</term>
<term>Antibody</term>
<term>Antibody neutralization</term>
<term>Antigenic</term>
<term>Antigenic drift</term>
<term>Antigenic shift</term>
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<term>Antigenic structure</term>
<term>Antigenic variation</term>
<term>Antigenic variations</term>
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<term>Bnabs</term>
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<term>Cleavage</term>
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<term>Multiple subtypes</term>
<term>Mutant</term>
<term>Mutation</term>
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<term>Neutralization epitopes</term>
<term>Neutralizing</term>
<term>Neutralizing antibodies</term>
<term>Neutralizing antibody</term>
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<term>Proteolytic cleavage</term>
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<term>Receptor binding</term>
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<term>Receptor binding site</term>
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<term>Ribbon diagram</term>
<term>Same color</term>
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<term>Structural basis</term>
<term>Structural information</term>
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<term>Subunit</term>
<term>Surface area</term>
<term>Universal vaccine</term>
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<term>Vaccine immunogens</term>
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<front><div type="abstract" xml:lang="en">Although seasonal influenza vaccines play a valuable role in reducing the spread of virus at the population level, ongoing viral evolution to evade immune responses remains problematic. No current vaccines elicit enduring protection in the face of emerging and re‐emerging influenza viruses that are rapidly undergoing antigenic drift. Eliciting broadly cross‐neutralizing antibody (nAb) responses against influenza virus is a crucial goal for seasonal and pandemic influenza vaccine preparation. Recent three‐dimensional structure information obtained from crystallization of influenza antigens in complex with nAbs has provided a framework for interpreting antibody‐based viral neutralization that should aid in the design of vaccine immunogens. Here, we will review current knowledge of the structure‐based mechanisms contributing to the neutralization and neutralization escape of influenza viruses. We will also explore the potential for this structure‐based approach to overcome the obstacles in developing the highly desired “universal” influenza vaccine.</div>
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Structural basis of influenza virus neutralization

Structural basis of influenza virus neutralization

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Abstract

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